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Information on EC 4.1.1.29 - sulfinoalanine decarboxylase and Organism(s) Mus musculus and UniProt Accession Q9DBE0
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4.1.1.29 sulfinoalanine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein. Also acts on L-cysteate. The 1992 edition of the Enzyme List erroneously gave the name sulfoalanine decarboxylase to this enzyme.
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Word Map
- 4.1.1.29
- dioxygenase
-
taut
- cystathionase
-
transsulfuration
-
taurine-deficient
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taurine-free
- nutrition
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cysteine sulfinic acid decarboxylase, cysteine sulfinate decarboxylase, cysteinesulfinate decarboxylase, cysteinesulfinic acid decarboxylase, cysteine-sulfinate decarboxylase, cgcsad1, undec1a, cgcsad2, l-cysteine sulfinate decarboxylase, csadcase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAD
-
-
-
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CADCase
-
-
-
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CSAD
CSAD/CAD
-
-
-
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CSADCase
-
-
-
-
CSD
Cysteic acid decarboxylase
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-
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Cysteic decarboxylase
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-
-
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Cysteine sulfinate decarboxylase
Cysteine sulfinic acid decarboxylase
Cysteine-sulfinate decarboxylase
Cysteinesulfinate decarboxylase
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-
-
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Cysteinesulfinic acid decarboxylase
Decarboxylase, cysteinesulfinate
-
-
-
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L-Cysteine sulfinate carboxy-lyase
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-
-
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L-Cysteinesulfinic acid decarboxylase
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-
-
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Sulfinoalanine decarboxylase
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-
-
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CSAD
-
-
-
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CSD
-
-
-
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Cysteine sulfinate decarboxylase
-
-
-
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Cysteine sulfinic acid decarboxylase
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-
-
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Cysteine-sulfinate decarboxylase
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-
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Cysteinesulfinic acid decarboxylase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
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SYSTEMATIC NAME
IUBMB Comments
3-sulfino-L-alanine carboxy-lyase (hypotaurine-forming)
A pyridoxal-phosphate protein. Also acts on L-cysteate. The 1992 edition of the Enzyme List erroneously gave the name sulfoalanine decarboxylase to this enzyme.
CAS REGISTRY NUMBER
COMMENTARY
62213-10-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Q8K566
rate-limiting enzyme for biosynthesis of taurine which is essential for biological processes such as development of the brain and eye, reproduction, osmoregulation as well as the anti-inflammatory activity of leukocytes
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-
?
additional information
?
-
-
rate-limiting enzyme for biosynthesis of taurine which is essential for biological processes such as development of the brain and eye, reproduction, osmoregulation as well as the anti-inflammatory activity of leukocytes
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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CSAD protein level increases during adipogenic differentiation of 3T3-L1 cells and is significantly increased when cells achieve a mature adipocyte phenotype
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
CSD is expressed in the glandular epithelium of the bulbourethral gland
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level of enzyme mRNA and protein increases from testis to epididymis to ductus deferens, main cell types containing enzyme are Leydig cells of testis, epithelial cells and some stromal cells
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CSD is expressed in the epithelial cells of the intermediate segments of prostate gland
CSD messenger RNA (mRNA) and protein are expressed in the major salivary glands of male mice. The relative levels of CSD mRNA increase from the submandibular gland (SMG) to the sublingual gland (SLG) and parotid gland (PG), but the levels of the CSD protein are the opposite
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CSD is expressed in the tall columnar cells of the seminal vesicle
additional information
the enzyme is mainly located in the excretory ducts (EDs) and interlobular duct (IL) of submandibular gland (SMG) and ED in sublingual gland (SLG), respectively. The relative levels of CSD mRNA increase from the submandibular gland (SMG) to the sublingual gland (SLG) and parotid gland (PG), but the levels of the CSD protein are the opposite. Immunofluorescence for the expression of CSD and alpha-SMA in SMG, SLG, and PG
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level of enzyme mRNA and protein increases from testis to epididymis to ductus deferens, main cell types containing enzyme are Leydig cells of testis, epithelial cells and some stromal cells
-
level of enzyme mRNA and protein increases from testis to epididymis to ductus deferens, main cell types containing enzyme are Leydig cells of testis, epithelial cells and some stromal cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
CSD is the rate-limiting enzyme of taurine biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CSAD_MOUSE
493
0
55145
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of CSAD knockout mice, chimeric CSAD KO mice are produced by injection of cells from a gene trap ES cell line (XP0392) into C57BL/6 (B6) blastocysts which are implanted into a pseudopregnant B6 mouse. Nine chimeric mice are mated with B6 in the animal colony. Agouti mice produced by this mating are back-crossed to B6 and offsprings are genotyped using PCR, overview. Although CSAD-/- generation (G)1 and G2 survive, offspring from G2 CSAD-/- have low brain and liver taurine concentrations and most die within 24 hrs of birth. Taurine concentrations in G3 CSAD-/- born from G2 CSAD-/- treated with taurine in the drinking water are restored and survival rates of G3 CSAD-/- increase from 15% to 92%. The mRNA expression of CDO, ADO, and TauT is not different in CSAD-/- compared to wild-type, and CSAD mRNA is not expressed in CSAD-/-. Expression of Gpx 1 and 3 is increased significantly in CSAD-/- and restored to normal levels with taurine supplementation. Lactoferrin and the prolactin receptor are significantly decreased in CSAD-/-. The prolactin receptor is restored with taurine supplementation
additional information
-
generation of CSAD knockout mice, chimeric CSAD KO mice are produced by injection of cells from a gene trap ES cell line (XP0392) into C57BL/6 (B6) blastocysts which are implanted into a pseudopregnant B6 mouse. Nine chimeric mice are mated with B6 in the animal colony. Agouti mice produced by this mating are back-crossed to B6 and offsprings are genotyped using PCR, overview. Although CSAD-/- generation (G)1 and G2 survive, offspring from G2 CSAD-/- have low brain and liver taurine concentrations and most die within 24 hrs of birth. Taurine concentrations in G3 CSAD-/- born from G2 CSAD-/- treated with taurine in the drinking water are restored and survival rates of G3 CSAD-/- increase from 15% to 92%. The mRNA expression of CDO, ADO, and TauT is not different in CSAD-/- compared to wild-type, and CSAD mRNA is not expressed in CSAD-/-. Expression of Gpx 1 and 3 is increased significantly in CSAD-/- and restored to normal levels with taurine supplementation. Lactoferrin and the prolactin receptor are significantly decreased in CSAD-/-. The prolactin receptor is restored with taurine supplementation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bile acids regulate cysteine sulfinic acid decarboxylase mRNA expression in a feedback fashion via mechanisms involving farnesoid X receptor small heterodimer partner Shp and farnesoid X receptor
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
mice supplemented with dietary cholate exhibit reduced hepatic cysteine sulfinic acid decarboxylase mRNA while those receiving cholestyramine exhibit increased mRNA. Activation of farnesoid X receptor suppresses cysteine sulfinic acid decarboxylase mRNA expression whereas cysteine sulfinic acid decarboxylase expression is increased in mice lacking farnesoid X receptor small heterodimer partner Shp. Hepatic hypotaurine concentration, the product of cysteine sulfinic acid decarboxylase, is higher in Shp-/- mice with a corresponding increase in serum taurine conjugated bile acids. Fibroblast growth factor 19 administration suppresses hepatic cholesterol 7-alpha-hydroxylase CYP7A1 mRNA but does not change cysteine sulfinic acid decarboxylase mRNA expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, E.; Park, S.Y.; Wang, C.; Xu, J.; LaFauci, G.; Schuller-Levis, G.
Cloning of murine cysteine sulfinic acid decarboxylase and its mRNA expression in murine tissues
Biochim. Biophys. Acta
1574
403-406
2002
Mus musculus (Q8K566), Mus musculus
Li, J.H.; Ling, Y.Q.; Fan, J.J.; Zhang, X.P.; Cui, S.
Expression of cysteine sulfinate decarboxylase (CSD) in male reproductive organs of mice
Histochem. Cell Biol.
125
607-613
2005
Mus musculus
Ueki, I.; Stipanuk, M.H.
3T3-L1 adipocytes and rat adipose tissue have a high capacity for taurine synthesis by the cysteine dioxygenase/cysteinesulfinate decarboxylase and cysteamine dioxygenase pathways
J. Nutr.
139
207-214
2009
Mus musculus
Fan, J.J.; Zhou, J.L.; Li, J.H.; Cui, S.
Accessory sex glands of male mice have the ability to synthesize taurine via the cysteine sulfinate decarboxylase pathway
Cell Biol. Int.
33
684-689
2009
Mus musculus
Kerr, T.; Matsumoto, Y.; Matsumoto, H.; Xie, Y.; Hirschberger, L.; Stipanuk, M.; Anakk, S.; Moore, D.; Watanabe, M.; Kennedy, S.; Davidson, N.
Cysteine sulfinic acid decarboxylase regulation: A role for farnesoid X receptor and small heterodimer partner in murine hepatic taurine metabolism
Hepatol. Res.
44
E218-228
2014
Mus musculus
Liu, S.; Liu, Y.; Ma, Q.; Cui, S.; Liu, J.
Expression and localization of cysteine sulfinate decarboxylase in major salivary glands of male mice
Arch. Oral Biol.
60
615-621
2015
Mus musculus (Q9DBE0)
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